The propagated properties of soliton transported bio-energy excited in the a-helix protein molecules with three channels in the cases of short-time and the long-time motion and its features of collision at temperature T=0 and biological temperature T=300K are studied numerically by the dynamic equations in the improved Davydov theory and fourth-order Runge-Kutta method, respectively. From these simulation experiments we see that the new solitons in the improved model can move without dispersion at a constant speed retaining its shape and energy in the cases of motion of both short-time or T=0 and long time or T=300K and can go through each other without scattering in their collisions. In these cases its lifetime is, at least, 120PS at 300K, in which the soliton can travel over about 700 amino acid residues. These results obtained are consistent with analytic result obtained by quantum perturbed theory in this model. In the meanwhile, the influences of structure disorder of a-helix protein molecules, including the inhomogeneous distribution of amino acids with different masses and fluctuations of spring constant, dipole-dipole interaction, exciton-phonon coupling constant and diagonal disorder, on the solitons are also studied by the fourth-order Runge-Kutta method. Therefore, the soliton still is very robust against the structure disorders and thermal perturbation of proteins at biological temperature 300K. Then we can conclude that the new soliton in in the a-helix protein molecules with three channels is a possible carrier of bio-energy transport and the improved model is possibly a candidate for the mechanism.